Component

TXN1

Independent protein record for Thioredoxin 1.

3 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. CRISPR–Cas9 silencing of TXN1 reduced IL-10-positive B-cell frequencies after CpGC stimulation.

    TXN1 → Human IL-10-positive regulatory B-cell differentiation source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Primary human B cells; 72-hour stimulation.
    limitations
    Supports machinery dependence, not selective drug targeting or evidence that a supplement causes autoimmunity.
    nutrient_topic
    Myricetin collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Myricetin
    plain_language
    Removing one component weakens the same immune program.
    primary_references
    Thioredoxin is a metabolic rheostat controlling regulatory B cells. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38553615/ · DOI 10.1038/s41590-024-01798-w
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Myricetin: metabolism, immune signaling, redox chemistry and cross-nutrient mechanisms (2026-09-19) · lines 308–314

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary human B cells; 72-hour stimulation. · source_derived_draft · unverified_draft

    ## myricetin-breg-silencing-txn1 Removing one component weakens the same immune program. CRISPR–Cas9 silencing of TXN1 reduced IL-10-positive B-cell frequencies after CpGC stimulation. Model: Primary human B cells; 72-hour stimulation. Limitations: Supports machinery dependence, not selective drug targeting or evidence that a supplement causes autoimmunity. Evidence access: Primary full text Thioredoxin is a metabolic rheostat controlling regulatory B cells. · 2024 · https://pubmed.ncbi.nlm.nih.gov/38553615/ · DOI 10.1038/s41590-024-01798-w
    Complete structured claim and evidence

What acts on it

  1. A rat TXNRD1 structure and docking model with human thioredoxin support a relay through the opposite subunit and C-terminal tail toward the substrate.

    Rat thioredoxin reductase 1 / Txnrd1 → TXN1 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    B2-dependent electron input and selenium-containing terminal chemistry are separate serial steps.
    evidence_location
    Abstract
    experimental_model
    Rat TXNRD1 Sec498Cys recombinant mutant with NADP+, 3.0-A crystallography and substrate-docking interpretation.
    exposure
    Purified-enzyme assay
    limitations
    Human thioredoxin was docked onto the rat Sec498Cys structure (Fig 6); the complex and cross-species turnover were not measured.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Rattus norvegicus reductase and Homo sapiens thioredoxin docking partner
    plain_language
    A second redox center carries electrons onward to thioredoxin.
    primary_references
    [sandalova2001] Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme. (2001). https://pubmed.ncbi.nlm.nih.gov/11481439/ DOI: 10.1073/pnas.171178698
    tissue_or_cell_type
    Purified recombinant enzyme; no intact tissue

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1360–1372

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Rat TXNRD1 Sec498Cys recombinant mutant with NADP+, 3.0-A crystallography and substrate-docking interpretation. · source_derived_draft · unverified_draft

    ### b2-txnrd1-terminal-relay A rat TXNRD1 structure and docking model with human thioredoxin support a relay through the opposite subunit and C-terminal tail toward the substrate. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: A second redox center carries electrons onward to thioredoxin. organism: Rattus norvegicus reductase and Homo sapiens thioredoxin docking partner tissue_or_cell_type: Purified recombinant enzyme; no intact tissue experimental_model: Rat TXNRD1 Sec498Cys recombinant mutant with NADP+, 3.0-A crystallography and substrate-docking interpretation. limitations: Human thioredoxin was docked onto the rat Sec498Cys structure (Fig 6); the complex and cross-species turnover were not measured. exposure: Purified-enzyme assay cross_nutrient: B2-dependent electron input and selenium-containing terminal chemistry are separate serial steps. evidence_location: Abstract [sandalova2001] Three-dimensional structure of a mammalian thioredoxin reductase: implications for mechanism and evolution of a selenocysteine-dependent enzyme. (2001). https://pubmed.ncbi.nlm.nih.gov/11481439/ DOI: 10.1073/pnas.171178698
    Complete structured claim and evidence

  2. Cytosolic TXNRD1 uses NADPH-derived reducing equivalents to reduce oxidized thioredoxin through its flavin and C-terminal redox centers.

    TXNRD1 → TXN1 source_derived_draftliterature_reviewed:direct_experimental
    Experimental context and source evidence
    experimental_model
    Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants.
    limitations
    This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit.
    organism
    Rat protein and recombinant enzyme assays

    Selenium: literature corrections and mechanism additions · lines 965–974

    Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants. · secondary_verified · secondary_verified

    ## txnrd1-reduces-txn1 TXNRD1 recharges thioredoxin so it can reduce other proteins. Cytosolic TXNRD1 uses NADPH-derived reducing equivalents to reduce oxidized thioredoxin through its flavin and C-terminal redox centers. Experimental model: Purified rat liver cytosolic thioredoxin reductase and recombinant active-site variants. Organism: Rat protein and recombinant enzyme assays Limitations: This experiment-specific relationship does not establish a human dietary-deficiency threshold or supplementation benefit. Primary reference: [Mammalian thioredoxin reductase: C-terminal redox center and selenium-to-sulfur substitution](https://pmc.ncbi.nlm.nih.gov/articles/PMC15961/)
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards